ArticleNeuropharmacology2015
Different sites of alcohol action in the NMDA receptor GluN2A and GluN2B subunits.
Article in Neuropharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Effect of Intravenous Ethanol on Capsaicin-Induced Hyperalgesia in Human Subjects.Alcoholism, clinical and experimental research · 2016Trial
- Naltrexone and Nalmefene as Modern Psychopharmacotherapy for Alcohol Use Disorder: Modulation of Opioid Receptors and Neurobiological Pathways of Alcohol Action.Biomedicines · 2026Review
- Impact of Prenatal Alcohol Exposure on the Cerebral Circulation: Potential Implications for Stroke.Advances in experimental medicine and biology · 2026Review
- Synaptic Effects Induced by Alcohol.Current topics in behavioral neurosciences · 2025Review
- Org24598, a Selective Glycine Transporter 1 (GlyT1) Inhibitor, Reverses Object Recognition and Spatial Memory Impairments Following Binge-like Ethanol Exposure in Rats.Molecules (Basel, Switzerland) · 2024Article
- Effects of ethanol on GluN1/GluN2A and GluN1/GluN2B NMDA receptor-ion channel gating kinetics.Alcoholism, clinical and experimental research · 2022Article
- Maternal Separation Alters Ethanol Drinking and Reversal Learning Processes in Adolescent Rats: The Impact of Sex and Glycine Transporter Type 1 (GlyT1) Inhibitor.International journal of molecular sciences · 2022Article
- Effects of Ethanol on Synaptic Plasticity and NMDA Currents in the Juvenile Rat Dentate Gyrus.Brain plasticity (Amsterdam, Netherlands) · 2020Article
- Chronic alcohol disrupts hypothalamic responses to stress by modifying CRF and NMDA receptor function.Neuropharmacology · 2020Article
- Positions in the N-methyl-D-aspartate Receptor GluN2C Subunit M3 and M4 Domains Regulate Alcohol Sensitivity and Receptor Kinetics.Alcoholism, clinical and experimental research · 2019Article
- GluN2B Subunit of the NMDA Receptor: The Keystone of the Effects of Alcohol During Neurodevelopment.Neurochemical research · 2019Review
- Implication of Genes for the N-Methyl-D-Aspartate (NMDA) Receptor in Substance Addictions.Molecular neurobiology · 2018Review
- Synaptic targets: Chronic alcohol actions.Neuropharmacology · 2017Review
- Two adjacent phenylalanines in the NMDA receptor GluN2A subunit M3 domain interactively regulate alcohol sensitivity and ion channel gating.Neuropharmacology · 2017Article
- Differential effects of TM4 tryptophan mutations on inhibition of N-methyl-d-aspartate receptors by ethanol and toluene.Alcohol (Fayetteville, N.Y.) · 2016Article
- N-Methyl-D-Aspartate Receptor Signaling and Function in Cardiovascular Tissues.Journal of cardiovascular pharmacology · 2016Review
- Intersubunit interactions at putative sites of ethanol action in the M3 and M4 domains of the NMDA receptor GluN1 and GluN2B subunits.British journal of pharmacology · 2016Article
- Disruption of S2-M4 linker coupling reveals novel subunit-specific contributions to N-methyl-d-aspartate receptor function and ethanol sensitivity.Neuropharmacology · 2016Article
- Gene Expression Changes in Glutamate and GABA-A Receptors, Neuropeptides, Ion Channels, and Cholesterol Synthesis in the Periaqueductal Gray Following Binge-Like Alcohol Drinking by Adolescent Alcohol-Preferring (P) Rats.Alcoholism, clinical and experimental research · 2016Article
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Authors and funding
4 authors.
Funding
Abstract
The NMDA receptor is a major target of alcohol action in the CNS, and recent behavioral and cellular studies have pointed to the importance of the GluN2B subunit in alcohol action. We and others have previously characterized four amino acid positions in the third and fourth membrane-associated (M) domains of the NMDA receptor GluN2A subunit that influence both ion channel gating and alcohol sensitivity. In this study, we found that substitution mutations at two of the four corresponding positions in the GluN2B subunit, F637 and G826, influence ethanol sensitivity and ion channel gating. Because position 826 contains a glycine residue in the native protein, we focused our attention on GluN2B(F637). Substitution mutations at GluN2B(F637) significantly altered ethanol IC50 values, glutamate EC50 values for peak (Ip) and steady-state (Iss) current, and steady-state to peak current ratios (Iss:Ip). Changes in apparent glutamate affinity were not due to agonist trapping in desensitized states, as glutamate Iss EC50 values were not correlated with Iss:Ip values. Ethanol sensitivity was correlated with values of both Ip and Iss glutamate EC50, but not with Iss:Ip. Values of ethanol IC50, glutamate EC50, and Iss:Ip for mutants at GluN2B(F637) were highly correlated with the corresponding values for mutants at GluN2A(F636), consistent with similar functional roles of this position in both subunits. These results demonstrate that GluN2B(Phe637) regulates ethanol action and ion channel function of NMDA receptors. However, despite highly conserved M domain sequences, ethanol's actions on GluN2A and GluN2B subunits differ.
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